Long, E. O. Regulation of immune responses through inhibitory receptors. Annu. Rev. Immunol.17, 875–904 (1999). ArticleCASPubMed Google Scholar
Tortorella, D., Gewurz, B. E., Furman, M. H., Schust, D. J. & Ploegh, H. L. Viral subversion of the immune system. Annu. Rev. Immunol.18, 861–926 (2000). ArticleCASPubMed Google Scholar
Algarra, I., Cabrera, T. & Garrido, F. The HLA crossroad in tumor immunology. Human Immunol.61, 65–73 (2000). ArticleCAS Google Scholar
Lanier, L. L., Corliss, B. & Phillips, J. H. Arousal and inhibition of human NK cells. Immunol. Rev.155, 145–154 (1997). ArticleCASPubMed Google Scholar
Isakov, N. Role of immunoreceptor tyrosine-based activation motif in signal transduction from antigen and Fc receptors. Adv. Immunol.69, 183–247 (1998). ArticleCASPubMed Google Scholar
Lanier, L. L., Yu, G. & Phillips, J. H. Analysis of FcgRIII (CD16) membrane expression and association with CD3ζ and FceRI-γ by site-directed mutation. J. Immunol.146, 1571–1576 (1991). CASPubMed Google Scholar
Wu, J., Cherwinski, H., Spies, T., Phillips, J. H. & Lanier, L. L. DAP10 and DAP12 form distinct, but functionally cooperative, receptor complexes in natural killer cells. J. Exp. Med.192, 1059–1068 (2000). ArticleCASPubMedPubMed Central Google Scholar
Lanier, L. L., Yu, G. & Phillips, J. H. Co-association of CD3ζ with a receptor (CD16) for IgG Fc on human natural killer cells. Nature342, 803–805 (1989). ArticleCASPubMed Google Scholar
Kurosaki, T. & Ravetch, J. V. A single amino acid in the glycosyl phosphatidylinositol attachment domain determines the membrane topology of FcγRIII. Nature342, 805–807 (1989). ArticleCASPubMed Google Scholar
Perussia, B. Signaling for cytotoxicity. Nature Immunol.1, 372–374 (2000). ArticleCAS Google Scholar
Perussia, B. et al. Human natural killer cells analyzed by B73.1, a monoclonal antibody blocking Fc receptor functions II. Studies of B73.1 antibody-antigen interaction on the lymphocyte membrane. J. Immunol.130, 2142–2148 (1983). CASPubMed Google Scholar
Lanier, L. L., Le, A. M., Phillips, J. H., Warner, N. L. & Babcock, G. F. Subpopulations of human natural killer cells defined by expression of the Leu-7 (HNK-1) and Leu-11 (NK-15) antigens. J. Immunol.131, 1789–1796 (1983). CASPubMed Google Scholar
Anegon, I., Cuturi, M. C., Trinchieri, G. & Perussia, B. Interaction of Fc receptor (CD16) ligands induces transcription of interleukin 2 receptors (CD25) and lymphokine genes and expression of their products in human natural killer cells. J. Exp. Med.167, 452–472 (1988). ArticleCASPubMed Google Scholar
Azzoni, L., Anegon, I., Calabretta, B. & Perussia, B. Ligand binding to FcgR induces c-_myc_-dependent apoptosis in IL-2-stimulated NK cells. J. Immunol.154, 491–499 (1995). CASPubMed Google Scholar
Ortaldo, J. R., Mason, A. T. & O'Shea, J. J. Receptor-induced death in human natural killer cells: Involvement of CD16. J. Exp. Med.181, 339–344 (1995). ArticleCASPubMed Google Scholar
Takai, T., Li, M., Sylvestre, D., Clynes, R. & Ravetch, J. V. FcR γ chain deletion results in pleiotropic effector cell defects. Cell76, 519–529 (1994). ArticleCASPubMed Google Scholar
Clynes, R. A., Towers, T. L., Presta, L. G. & Ravetch, J. V. Inhibitory Fc receptors modulate in vivo cytotoxicity against tumor targets. Nature Med.6, 443–446 (2000). ArticleCASPubMed Google Scholar
Arase, N. et al. Association with FcRγ is essential for activation signal through NKR-P1 (CD161) in natural killer (NK) cells and NK1.1+ T cells. J. Exp. Med.186, 1957–1963 (1997). ArticleCASPubMedPubMed Central Google Scholar
Pessino, A. et al. Molecular cloning of NKp46: a novel member of the immunoglobulin superfamily involved in triggering of natural cytotoxicity. J. Exp. Med.188, 953–960 (1998). ArticleCASPubMedPubMed Central Google Scholar
Pende, D. et al. Identification and molecular characterization of NKP30, a novel triggering receptor involved in natural cytotoxicity mediated by human natural killer cells. J. Exp. Med.190, 1505–1516 (1999). ArticleCASPubMedPubMed Central Google Scholar
Tomasello, E. et al. Association of signal-regulatory proteins beta with KARAP/DAP-12. Eur. J. Immunol.30, 2147–2156 (2000). ArticleCASPubMed Google Scholar
Colucci, F. et al. Redundant role of the Syk protein tyrosine kinase in mouse NK cell differentiation. J. Immunol.163, 1769–1774 (1999). CASPubMed Google Scholar
Lanier, L. L., Corliss, B. C., Wu, J., Leong, C. & Phillips, J. H. Immunoreceptor DAP12 bearing a tyrosine-based activation motif is involved in activating NK cells. Nature391, 703–707 (1998). ArticleCASPubMed Google Scholar
Olcese, L. et al. Human killer cell activatory receptors for MHC class I molecules are included in a multimeric complex expressed by natural killer cells. J. Immunol.158, 5083–5086 (1997). CASPubMed Google Scholar
Lanier, L. L., Corliss, B., Wu, J. & Phillips, J. H. Association of DAP12 with activating CD94/NKG2C NK cell receptors. Immunity8, 693–701 (1998). ArticleCASPubMed Google Scholar
Smith, K. M., Wu, J., Bakker, A. B. H., Phillips, J. H. & Lanier, L. L. Ly49D and Ly49H associate with mouse DAP12 and form activating receptors. J. Immunol.161, 7–10 (1998). CASPubMed Google Scholar
Vitale, M. et al. NKp44, a novel triggering surface molecule specifically expressed by activated natural killer cells, is involved in non-major histocompatibility complex-restricted tumor cell lysis. J. Exp. Med.187, 2065–2072 (1998). ArticleCASPubMedPubMed Central Google Scholar
Bakker, A. B., Baker, E., Sutherland, G. R., Phillips, J. H. & Lanier, L. L. Myeloid DAP12-associating lectin (MDL)-1 is a cell surface receptor involved in the activation of myeloid cells. Proc. Natl Acad. Sci. USA96, 9792–9796 (1999). ArticleCASPubMedPubMed Central Google Scholar
Dietrich, J., Cella, M., Seiffert, M., Buhring, H. J. & Colonna, M. Cutting edge: signal-regulatory protein β1 is a DAP12-associated activating receptor expressed in myeloid cells. J. Immunol.164, 9–12 (2000). ArticleCASPubMed Google Scholar
Bouchon, A., Dietrich, J. & Colonna, M. Cutting edge: inflammatory responses can Be triggered by TREM-1, a novel receptor expressed on neutrophils and monocytes. J. Immunol.164, 4991–4995 (2000). ArticleCASPubMed Google Scholar
McVicar, D. W. et al. DAP12-mediated signal transduction in natural killer cells. A dominant role for the syk protein-tyrosine kinase. J. Biol. Chem.273, 32934–32942 (1998). ArticleCASPubMed Google Scholar
Braud, V. M. et al. HLA-E binds to natural killer cell receptors CD94/NKG2A, B, and C. Nature391, 795–798 (1998). ArticleCASPubMed Google Scholar
Vance, R. E., Jamieson, A. M. & Raulet, D. H. Recognition of the Class Ib molecule Qa-1b by putative activating receptors CD94/NKG2C and CD94/NKG2E on mouse natural killer cells. J. Exp. Med.190, 1801–1812 (1999). ArticleCASPubMedPubMed Central Google Scholar
George, T. C., Ortaldo, J. R., Lemieux, S., Kumar, V. & Bennett, M. Tolerance and Alloreactivity of the Ly49D Subset of Murine NK Cells. J. Immunol.163, 1859–1867 (1999). CASPubMed Google Scholar
Idris, A. H. et al. The natural killer gene complex genetic locus Chok encodes Ly-49D, it target recognition receptor that activates natural killing. Proc. Natl Acad. Sci. USA96, 6330–6335 (1999). ArticleCASPubMedPubMed Central Google Scholar
Nakamura, M. C. et al. Natural killing of xenogeneic cells mediated by the mouse Ly-49D receptor. J. Immunol.163, 4694–700 (1999). CASPubMed Google Scholar
Winter, C. C., Gumperz, J. E., Parham, P., Long, E. O. & Wagtmann, N. Direct binding and functional transfer of NK cell inhibitory receptors reveal novel patterns of HLA-C allotype recognition. J. Immunol.161, 571–577 (1998). CASPubMed Google Scholar
Valés-Gómez, M., Reyburn, H. T., Erskine, R. A., Lopez-Botet, M. & Strominger, J. L. Kinetics and peptide dependency of the binding of the inhibitory NK receptor CD94/NKG2-A and the activating receptor CD94/NKG2-C to HLA-E. EMBO J.18, 4250–4260 (1999). ArticlePubMedPubMed Central Google Scholar
Tomasello, E. et al. Combined Natural Killer Cell and Dendritic Cell Functional Deficiency in KARAP/DAP12 Loss-of-Function Mutant Mice. Immunity13, 355–364 (2000). ArticleCASPubMed Google Scholar
Bakker, A.B.H. et al. DAP12-deficient mice fail to develop autoimmunity due to impaired antigen priming. Immunity13, 345–353 (2000). ArticleCASPubMed Google Scholar
Paloneva, J. et al. Loss-of-function mutations in TYROBP (DAP12) result in a presenile dementia with bone cysts. Nature Genet.25, 357–361 (2000). ArticleCASPubMed Google Scholar
Jiang, K. et al. Pivotal role of phosphoinositide-3 kinase in regulation of cytotoxicity in natural killer cells. Nature Immunol.1, 419–425 (2000). ArticleCAS Google Scholar
Wu, J. et al. An activating receptor complex on natural killer and T cells formed by NKG2D and DAP10. Science285, 730–732 (1999). ArticleCASPubMed Google Scholar
Houchins, J. P., Yabe, T., McSherry, C. & Bach, F. H. DNA sequence analysis of NKG2, a family of related cDNA clones encoding type II integral membrane proteins on human natural killer cells. J. Exp. Med.173, 1017–1020 (1991). ArticleCASPubMed Google Scholar
Songyang, Z. et al. SH2 domains recognize specific phosphopeptide sequences. Cell72, 767–778 (1996). Google Scholar
Chang, C. et al. Cutting edge: KAP10, a novel transmembrane adapter protein genetically linked to DAP12 but with unique signaling properties. J. Immunol.163, 4651–4654 (1999). CASPubMed Google Scholar
Bauer, S. et al. Activation of natural killer cells and T cells by NKG2D, a receptor for stress-inducible MICA. Science285, 727–730 (1999). ArticleCASPubMed Google Scholar
Berg, S. F., Dissen, E., Westgaard, I. H. & Fossum, S. Molecular characterization of rat NKR-P2, a lectin-like receptor expressed by NK cells and resting T cells. Int. Immunol.10, 379–385 (1998). ArticleCASPubMed Google Scholar
Ho, E. L. et al. Murine Nkg2d and Cd94 are clustered within the natural killer complex and are expressed independently in natural killer cells. Proc. Natl Acad. Sci. USA95, 6320–6325 (1998). ArticleCASPubMedPubMed Central Google Scholar
Bahram, S., Bresnahan, M., Geraghty, D. E. & Spies, T. A second lineage of mammalian major histocompatibility complex class I genes. Proc. Natl Acad. Sci. USA91, 6259–6263 (1994). ArticleCASPubMedPubMed Central Google Scholar
Li, P. et al. Crystal structure of the MHC class I homolog MIC–A, a γδT cell ligand. Immunity10, 577–584 (1999). ArticleCASPubMed Google Scholar
Groh, V. et al. Cell stress-regulated human major histocompatibility complex class I gene expressed in gastrointestinal epithelium. Proc. Natl Acad. Sci. USA93, 12445–12450 (1996). ArticleCASPubMedPubMed Central Google Scholar
Groh, V. et al. Broad tumor-associated expression and recognition by tumor-derived gamma delta T cells of MICA and MICB. Proc. Natl Acad. Sci. USA96, 6879–6884 (1999). ArticleCASPubMedPubMed Central Google Scholar
Nomura, M. et al. Genomic structures and characterization of Rae1 family members encoding GPI-anchored cell surface proteins and expressed predominantly in embryonic mouse brain. J. Biochem.120, 987–995 (1996). ArticleCASPubMed Google Scholar
Nomura, M., Takihara, Y. & Shimada, K. Isolation and characterization of retinoic acid-inducible cDNA clones in F9 cells: one of the early inducible clones encodes a novel protein sharing several highly homologous regions with a Drosophila polyhomeotic protein. Differentiation57, 39–50 (1994). ArticleCASPubMed Google Scholar
Malarkannan, S. et al. The molecular and functional characterization of a dominant minor H antigen, H60. J. Immunol.161, 3501–3509 (1998). CASPubMed Google Scholar
Cerwenka, A. et al. Retinoic acid early inducible genes define a ligand family for the activating NKG2D receptor in mice. Immunity12, 721–727 (2000). ArticleCASPubMed Google Scholar
Diefenbach, A., Jamieson, A.M., Liu, S.D., Shastri, N. & Raulet, D.H. Ligands for the murine NKG2D receptor: expression by tumor cells and activation of NK cells and macrophages. Nature Immunol.1, 119–126 (2000). ArticleCAS Google Scholar
Chalupny, J. et al. Soluble forms of the novel MHC class I-related molecules, ULBP1 and ULBP2, bind to and functionally activate NK cells. FASEB J.14, 1018 (2000). Google Scholar
Lenschow, D.J., Walunas, T.L. & Bluestone, J.A. CD28/B7 system of T cell costimulation. Annu. Rev. Immunol.14, 233–258 (1996). ArticleCASPubMed Google Scholar
Chambers, C.A. & Allison, J.P. Costimulatory regulation of T cell function. Curr. Opin. Cell. Biol.11, 203–210 (1999). ArticleCASPubMed Google Scholar
Prasad, K.V. et al. T-cell antigen CD28 interacts with the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr (P)-Met-Xaa-Met motif. Proc. Natl Acad. Sci. USA91, 2834–2838 (1994). ArticleCASPubMedPubMed Central Google Scholar
Truitt, K. E., Hicks, C. M. & Imboden, J. B. Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat T cells. J. Exp. Med.179, 1071–1076 (1994). ArticleCASPubMed Google Scholar
Pages, F. et al. Binding of phosphatidyl-inositol-3-OH kinase to CD28 is required for T-cell signalling. Nature369, 3327–3329 (1994). Article Google Scholar
Stein, P. H., Fraser, J. D. & Weiss, A. The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidylinositol 3′-kinase. Mol. Cell. Biol.14, 3392–3402 (1994). ArticleCASPubMedPubMed Central Google Scholar
Truitt, K. E. et al. CD28 delivers costimulatory signals independently of its association with phosphatidylinositol 3-kinase. J. Immunol.155, 4702–4710 (1995). CASPubMed Google Scholar
Ni, H.-T., Deeths, M. J. & Mescher, M. F. Phosphatidylinositol 3 kinase activity is not essential for B7-1-mediated costimulation of proliferation or development of cytotoxicity in murine T cells. J. Immunol.157, 2243–2246 (1996). CASPubMed Google Scholar
Cai, Y.-C. et al. Selective CD28 pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation. Immunity3, 417–426 (1995). ArticleCASPubMed Google Scholar
Nandi, D., Gross, J.A. & Allison, J.P. CD28-mediated costimulation is necessary for optimal proliferation of murine NK cells. J. Immunol.152, 3361–3369 (1994). CASPubMed Google Scholar
Heldhof, A.B. et al. Expression of B7–1 by highly metastatic mouse T lymphomas induces optimal natural killer cell-mediated cytotoxicity. Cancer Res.55, 2730–2733 (1995). Google Scholar
Chambers, B. J., Salcedo, M. & Ljunggren, H.-G. Triggering of natural killer cells by the costimulatory molecule CD80 (B7-1). Immunity5, 311–317 (1996). ArticleCASPubMed Google Scholar
Hunter, C. A. et al. The role of the CD28/B7 interaction in regulation of NK cell responses during infection with Toxoplasma gondii. J. Immunol.158, 2285–2293 (1997). CASPubMed Google Scholar
Azuma, M., Cayabyab, M., Buck, D., Phillips, J. H. & Lanier, L. L. Involvement of CD28 in major histocompatibility complex-unrestricted cytotoxicity mediated by a human NK leukemia cell line. J. Immunol.149, 1115–1123 (1992). CASPubMed Google Scholar
Lanier, L. L. et al. CD80 (B7) and CD86 (B70) provide similar costimulatory signals for T cell proliferation, cytokine production, and generation of CTL. J. Immunol.154, 97–105 (1995). CASPubMed Google Scholar
Galea-Lauri, J. et al. Expression of a variant of CD28 on a subpopulation of human NK cells: implications for B7-mediated stimulation of NK cells. J. Immunol.163, 62–70 (1999). CASPubMed Google Scholar
Garni-Wagner, B. A., Purohit, A., Mathew, P. A., Bennett, M. & Kumar, K. A novel function-associated molecule related to non-MHC-restricted cytotoxicity mediated by activated natural killer cells and T cells. J. Immunol.151, 60–70 (1993). CASPubMed Google Scholar
Mathew, P. A. et al. Cloning and characterization of the 2B4 gene encoding a molecule associated with non-MHC-restricted killing mediated by activated natural killer cells and T cells. J. Immunol.151, 5328–5337 (1993). CASPubMed Google Scholar
Poy, F. et al. Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition. Mol. Cell4, 555–561 (1999). ArticleCASPubMed Google Scholar
Cocks, B. G. et al. A novel receptor involved in T-cell activation. Nature376, 260–263 (1995). ArticleCASPubMed Google Scholar
Sayos, J. et al. The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM. Nature395, 462–469 (1998). ArticleCASPubMed Google Scholar
Nichols, K. E. et al. Inactivating mutations in an SH2 domain-encoding gene in X-linked lymphoproliferative syndrome. Proc. Natl Acad. Sci. USA95, 13765–13770 (1998). ArticleCASPubMedPubMed Central Google Scholar
Seemayer, T. A. et al. X-linked lymphoproliferative disease: Twenty-five years after the discovery. Pediatr. Res.38, 471–478 (1999). Article Google Scholar
Brown, M. H. et al. 2B4, the Natural Killer and T Cell Immunoglobulin Superfamily Surface Protein, Is a Ligand for CD48. J. Exp. Med.188, 2083–2090 (1998). ArticleCASPubMedPubMed Central Google Scholar
Latchman, Y., McKay, P. F. & Reiser, H. Identification of the 2B4 molecule as a counter-receptor for CD48. J. Immunol.161, 5809–5812 (1998). CASPubMed Google Scholar
Yokoyama, S. et al. Expression of the BLAST-1 activation/adhesion molecule and its identification as CD48. J. Immunol.146, 2192–2200 (1991). CASPubMed Google Scholar
Klaman, L. D. & Thorley-Lawson, D. A. Characterization of the CD48 gene demonstrates a positive element that is specific to Epstein-Barr virus-immortalized B-cell lines and contains an essential NF-κB site. J. Virol.69, 871–881 (1995). CASPubMedPubMed Central Google Scholar
Valiante, N. M. & Trinchieri, G. Identification of a novel signal transduction surface molecule on human cytotoxic lymphocytes. J. Exp. Med.178, 1397–1406 (1993). ArticleCASPubMed Google Scholar
Tangye, S. G., Phillips, J. H., Lanier, L. L. & Nichols, K. E. Cutting edge: functional requirement for SAP in 2B4-mediated activation of human natural killer cells as revealed by the X-linked lymphoproliferative syndrome. J. Immunol.165, 2932–2936 (2000). ArticleCASPubMed Google Scholar
Sivori, S. et al. 2B4 functions as a co-receptor in human NK cell activation. Eur. J. Immunol.30, 787–793 (2000). ArticleCASPubMed Google Scholar
Nakajima, H., Cella, M., Langen, H., Friedlein, A. & Colonna, M. Activating interactions in human NK cell recognition: the role of 2B4-CD48. Eur. J. Immunol.29, 1676–1683 (1999). ArticleCASPubMed Google Scholar
Tangye, S. G. et al. Human 2B4, an activating NK cell receptor, recruits the protein tyrosine phosphatase SHP-2 and the adaptor signaling protein SAP. J. Immunol.162, 6981–6985 (1999). CASPubMed Google Scholar
Watzl, C., Stebbins, C. C. & Long, E. O. NK cell inhibitory receptors prevent tyrosine phosphorylation of the activation receptor 2B4 (CD244). J. Immunol.165, 3545–3548 (2000). ArticleCASPubMed Google Scholar
Kubin, M. Z. et al. Molecular cloning and biological characterization of NK cell activation- inducing ligand, a counterstructure for CD48. Eur. J. Immunol.29, 3466–3477 (1999). ArticleCASPubMed Google Scholar
Parolini, S. et al. X-linked lymphoproliferative disease. 2B4 molecules displaying inhibitory rather than activating function are responsible for the inability of natural killer cells to kill Epstein-Barr virus-infected cells. J. Exp. Med.192, 337–346 (2000). ArticleCASPubMedPubMed Central Google Scholar
Benoit, L., Wang, X., Pabst, H. F., Dutz, J. & Tan, R. Defective NK cell activation in X-linked lymphoproliferative disease. J. Immunol.165, 3549–3553 (2000). ArticleCASPubMed Google Scholar
Nakajima, H. et al. Patients with X-linked lymphoproliferative disease have a defect in 2B4 receptor-mediated NK cell cytotoxicity. Eur. J. Immunol.30, 3309–3318 (2000). ArticleCASPubMed Google Scholar
Gonzalez-Cabrero, J. et al. CD48-deficient mice have a pronounced defect in CD4+ T cell activation. Proc. Natl Acad. Sci. USA96, 1019–1023 (1999). ArticleCASPubMedPubMed Central Google Scholar
Schuhmachers, G. et al. Activation of murine epidermal γδT cells through surface 2B4. Eur. J. Immunol.25, 1117–1120 (1995). ArticleCASPubMed Google Scholar